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H9916 Sigma

HRV3C Protease

recombinant, expressed in E. coli, ≥99% (SDS-PAGE)

Synonym: Human Rhinovirus 3C Protease

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Properties

Related Categories Application Index, Biochemicals and Reagents, Enzymes, Inhibitors, and Substrates, Proteases & Protein Sequencing, Proteases for Recombinant Protein Fusion Tag Cleavage More...
recombinant   expressed in E. coli
description   For cleavage of fusion proteins containing LeuGluValLeuPheGln/GlyPro sequence
assay   ≥99% (SDS-PAGE)
form   liquid
activity   ≥1 units/μg
storage temp.   −20°C

Description

Application

Human rhinovirus 3C protease (HRV3C Protease) is a cysteine protease that recognizes the cleavage site of Leu-Glu-Val-Leu-Phe-Gln*Gly-Pro. Supplied as a 47 kDa protein with both GST and Histidine tags for easy removal by His-Select or Glutathione agarose along with the cleaved tag.

HRV3C Protease has a therapeutic implication because of its unique protein structure. It may be used for the biochemical and structural characterization conducted on HRV 3C protease along with the development of 3C protease inhibitors.

Preparation Note

It is recommended to use HRV3C Protease at a protease-to-target protein ratio of 1:100 (w/w) or 1 unit of HRV3C Protease to 100 μg of target protein in a buffer suitable for the target protein at 4 °C overnight, with the target protein concentration at 1-2 mg/ml. In most cases, target proteins are completely cleaved with a protease to target protein ratio of 1:50 to 1:400, or 1 unit HRV3C Protease to 50-400 μg of target protein. The efficiency of cleavage may vary due to the sequences around the cleavage site, conformation and the solubility of the target protein. Due to its high specificity, more HRV3C Protease (at 1:10 ratio) or longer cleavage time at higher temperature (37 °C) can be used to achieve high cleavage efficiency without non-specific cleavage of target proteins.

Physical form

Supplied as a solution in 25 mM Tris-HCl, pH 8.0, 50 mM NaCl, 1 mM TCEP and 50% glycerol

Biochem/physiol Actions

Human rhinovirus 3C protease (HRV3C Protease) is a cysteine protease that recognizes the cleavage site of Leu-Glu-Val-Leu-Phe-Gln*Gly-Pro. It is supplied as a 47 kDa protein with both GST and Histidine tags for easy removal by His-Select or Glutathione agarose along with the cleaved tag. HRV3C Protease is capable of cleaving small peptides with the sequence of polyprotein processing sites. It cleaves after the glutamine residue. HRV cleavage site generally contains Gln/Gly scissile bond.

General description

HRV3C Protease is a recombinant restriction-grade cysteine protease. It folds into two topologically alike six-stranded β barrels. However, β barrels are different in length and individual position as well as in loops connecting elements of secondary structure. The protease is distinguishable from others by the fact that it has a cysteine nucleophile but with a chymotrypsin-like serine protease folding.

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Biomedical Applications
Safety & Documentation

Safety Information

RIDADR 
NONH for all modes of transport
WGK Germany 
2

Documents

Certificate of Analysis

Certificate of Origin

Protocols & Articles
Peer-Reviewed Papers
15

References

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